A bifunctional protein consisting of aspartokinase, and homoserine dehydrogenase activities. It is found primarily in BACTERIA and in PLANTS.
An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.
An enzyme that catalyzes the formation of beta-aspartyl phosphate from aspartic acid and ATP. Threonine serves as an allosteric regulator of this enzyme to control the biosynthetic pathway from aspartic acid to threonine. EC 2.7.2.4.
An enzyme that catalyzes the conversion of L-aspartate 4-semialdehyde, orthophosphate, and NADP+ to yield L-4-aspartyl phosphate and NADPH. EC 1.2.1.11.
An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria found in soil, water, food, and clinical specimens. It is a prominent opportunistic pathogen for hospitalized patients.
One of the FURANS with a carbonyl thereby forming a cyclic lactone. It is an endogenous compound made from gamma-aminobutyrate and is the precursor of gamma-hydroxybutyrate. It is also used as a pharmacological agent and solvent.
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
A genus of asporogenous bacteria that is widely distributed in nature. Its organisms appear as straight to slightly curved rods and are known to be human and animal parasites and pathogens.
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The first enzyme in the METHIONINE biosynthetic pathway, this enzyme catalyzes the succinylation reaction of L-homoserine to O-succinyl-L-homoserine and COENZYME A using succinyl-CoA.
Cyclic esters of acylated BUTYRIC ACID containing four carbons in the ring.
A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
The rate dynamics in chemical or physical systems.
The functional hereditary units of BACTERIA.
A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
A series of oxidative reactions in the breakdown of acetyl units derived from GLUCOSE; FATTY ACIDS; or AMINO ACIDS by means of tricarboxylic acid intermediates. The end products are CARBON DIOXIDE, water, and energy in the form of phosphate bonds.
Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7.
An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.
A genus of VIBRIONACEAE, made up of short, slightly curved, motile, gram-negative rods. Various species produce cholera and other gastrointestinal disorders as well as abortion in sheep and cattle.
The order Actiniaria, in the class ANTHOZOA, comprised of large, solitary polyps. All species are carnivorous.
The pattern of GENE EXPRESSION at the level of genetic transcription in a specific organism or under specific circumstances in specific cells.
The relationship between two different species of organisms that are interdependent; each gains benefits from the other or a relationship between different species where both of the organisms in question benefit from the presence of the other.
Flagellate EUKARYOTES, found mainly in the oceans. They are characterized by the presence of transverse and longitudinal flagella which propel the organisms in a rotating manner through the water. Dinoflagellida were formerly members of the class Phytomastigophorea under the old five kingdom paradigm.
A phylum of radially symmetrical invertebrates characterized by possession of stinging cells called nematocysts. It includes the classes ANTHOZOA; CUBOZOA; HYDROZOA, and SCYPHOZOA. Members carry CNIDARIAN VENOMS.
The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.
Processes occurring in various organisms by which new genes are copied. Gene duplication may result in a MULTIGENE FAMILY; supergenes or PSEUDOGENES.
A mechanism of communication with a physiological system for homeostasis, adaptation, etc. Physiological feedback is mediated through extensive feedback mechanisms that use physiological cues as feedback loop signals to control other systems.
The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES.

Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine. (1/18)

The regulatory domain of the bifunctional threonine-sensitive aspartate kinase homoserine dehydrogenase contains two homologous subdomains defined by a common loop-alpha helix-loop-beta strand-loop-beta strand motif. This motif is homologous with that found in the two subdomains of the biosynthetic threonine-deaminase regulatory domain. Comparisons of the primary and secondary structures of the two enzymes allowed us to predict the location and identity of the amino acid residues potentially involved in two threonine-binding sites of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase. These amino acids were then mutated and activity measurements were carried out to test this hypothesis. Steady-state kinetic experiments on the wild-type and mutant enzymes demonstrated that each regulatory domain of the monomers of aspartate kinase-homoserine dehydrogenase possesses two nonequivalent threonine-binding sites constituted in part by Gln(443) and Gln(524). Our results also demonstrated that threonine interaction with Gln(443) leads to inhibition of aspartate kinase activity and facilitates the binding of a second threonine on Gln(524). Interaction of this second threonine with Gln(524) leads to inhibition of homoserine dehydrogenase activity.  (+info)

Isolation of the aspartokinase domain of bifunctional aspartokinase I-homoserine dehydrogenase I from E.coli K12. (2/18)

A proteolytic fragment (Mr approximately 25 000) carrying only the aspartokinase activity has been purified by chromatofocusing after limited proteolysis of aspartokinase I-homoserine dehydrogenase I from E.coli K12. The NH2-terminal sequence shows that it corresponds to the amino terminal peptide of the native enzyme. The results confirm a previous hypothesis about the organization of native aspartokinase I-homoserine dehydrogenase I.  (+info)

Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. Structural and evolutionary relationships with Escherichia coli aspartokinases-homoserine dehydrogenases I and II. (3/18)

The Bacillus subtilis hom gene, encoding homoserine dehydrogenase (L-homoserine:NADP+ oxidoreductase, EC 1.1.1.3) has been cloned and its nucleotide sequence determined. The B. subtilis enzyme expressed in Escherichia coli is sensitive by inhibition by threonine and allows complementation of a strain lacking homoserine dehydrogenases I and II. Nucleotide sequence analysis indicates that the hom stop codon overlaps the start codon of thrC (threonine synthase) suggesting that these genes, as well as thrB (homoserine kinase) located downstream from thrC, belong to the same transcription unit. The deduced amino acid sequence of the B. subtilis homoserine dehydrogenase shows extensive similarity with the C-terminal part of E. coli aspartokinases-homoserine dehydrogenases I and II; this similarity starts at the exact point where the similarity between E. coli or B. subtilis aspartokinases and E. coli aspartokinases-homoserine dehydrogenases stops. These data suggest that the E. coli bifunctional polypeptide could have resulted from the direct fusion of ancestral aspartokinase and homoserine dehydrogenase. The B. subtilis homoserine dehydrogenase has a C-terminal extension of about 100 residues (relative to the E. coli enzymes) that could be involved in the regulation of the enzyme activity.  (+info)

Subunit structure of the methionine-repressible aspartokinase II--homoserine dehydrogenase II from Escherichia coli K12. (4/18)

The quaternary structure of Escherichia coli K12 aspartokinase II--homoserine dehydrogenase II has been examined. This multifunctional protein has a molecular weight Mr = 176000. It is composed of two subunits having the same molecular weight and the same charge. The results obtained from the examination of tryptic maps, the number and amino acid composition of cysteine-containing peptides and the uniqueness of the N-terminal sequence, strongly suggest that the 2 subunits are identical. The properties of aspartokinase II--homoserine dehydrogenase II can be compared to those of the much better known protein aspartokinase I--homoserine dehydrogenase I.  (+info)

Threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Kinetic and spectroscopic effects upon binding of serine and threonine. (5/18)

The two threonine-sensitive activities aspartokinase and homoserine dehydrogenase are inhibited by L-serine. The inhibition of the aspartokinase by L-serine displays homotropic cooperative effects and is competitive versus aspartate. The inhibition by L-serine of the homoserine dehydrogenase displays Michaelis-Menten kinetics which are of a competitive nature versus homoserine. Characteristic effects of L-serine on the protein include a perturbation of its absorption and fluorescence spectra, with an increase in the fluorescence of the protein-NADPH complex. L-serine shifts the allosteric equilibrium of the protein to a "T-like" conformation to which L-threonine binds noncooperatively. L-Serine, a threonine analog, is not capable, as the physiological effector, of inducing a complete R to T transition of the enzyme; the aspartokinase globules show a cooperative conformation change upon serine binding, but this conformation change is not found in the homoserine dehydrogenase globules.  (+info)

Proteolysis of the bifunctional methionine-repressible aspartokinase II-homoserine dehydrogenase II of Escherichia coli K12. Production of an active homoserine dehydrogenase fragment. (6/18)

The dimeric bifunctional enzyme aspartokinase II-homoserine dehydrogenase II (Mr = 2 X 88,000) of Escherichia coli K12 can be cleaved into two nonoverlapping fragments by limited proteolysis with subtilisin. These two fragments can be separated under nondenaturing conditions as dimeric species, which indicates that each fragment has retained some of the association areas involved in the conformation of the native protein. The smaller fragment (Mr = 2 X 24,000) is devoid of aspartokinase and homoserine dehydrogenase activity. The larger fragment (Mr = 2 X 37,000) is endowed with full homoserine dehydrogenase activity. These results show that the polypeptide chains of the native enzyme are organized in two different domains, that both domains participate in building up the native dimeric structure, and that one of these domains only is responsible for homoserine dehydrogenase activity. A model of aspartokinase II-homoserine dehydrogenase II is proposed, which accounts for the present results.  (+info)

The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Carboxymethylation of the enzyme: threonine binding and inhibition are functionally dissociable. (7/18)

The inactivation of the aspartokinase I-homoserine dehydrogenase I by iodoacetic acid and the effect on the sensitivity to its inhibitor, L-threonine, were examined. Both aspartokinase and homoserine dehydrogenase inactivation, as well as the dehydrogenase desensitization toward L-threonine occur as a pseudo-first order process. During its inactivation, the aspartokinase remains sensitive to L-threonine. At 50% inactivation, the inhibition curve of the aspartokinase by L-threonine displays homotropic cooperative effects. This alkylated protein retains eight binding sites for L-threonine. During the carboxymethylation, the protein remains in the tetrameric form until half of the kinase activity is lost. At the end of the inactivation aggregate forms and dimers appear.  (+info)

The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Site of limited proteolytic cleavage by subtilisin. (8/18)

The sequence of the first 25 residues of the homoserine dehydrogenase fragment, produced by limited proteolysis of aspartokinase I-homoserine dehydrogenase I with substilisin, has been determined. The sequence of a cyanogen bromide peptide (CB5, 59 residues), isolated from the entire protein, is also presented. Residues 1 to 18 of the subtilisin homoserine dehydrogenase fragment match the sequence 42 to 59 of peptide CB5.  (+info)

cd04881 (PSSM ID: 153153): Conserved Protein Domain Family ACT_HSDH-Hom, The ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) encoded by the hom gene of Bacillus subtilis and other related sequences
K00928 lysC; aspartate kinase [EC:2.7.2.4] K00928 lysC; aspartate kinase [EC:2.7.2.4] K00928 lysC; aspartate kinase [EC:2.7.2.4] K12524 thrA; bifunctional aspartokinase / homoserine dehydrogenase 1 [EC:2.7.2.4 1.1.1.3] K12525 metL; bifunctional aspartokinase / homoserine dehydrogenase 2 [EC:2.7.2.4 1.1.1.3 ...
Introduction: Aspartokinase (A1, A2, A3) Homoserine dehydrogenase (B1, B2) Threonine dehydratase (C1, C2) Allosteric regulation of selective isozymes some unregulated Sequential feedback inhibition Same product inhibits its biosynthetic path at multiple sites Inhibits first enzyme in pathway
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Dr Allan Goldman trained as a doctor in South Africa before coming to London in 1990. He completed his paediatric intensive care specialisation in both London and Australia. He took up the post of consultant at Great Ormond Street Hospital (GOSH) in 1998. ...
Numerous hits in gapped BLAST to NADH dehydrogenase I chain A / NADH-ubiquinone oxidoreductase sequences,e.g.residues 1-118 are 55% similar to NADH-ubiquinone dehydrogenase chain A 1 from Mesorhizobium loti (14022149,).Residues 6-117 are 32% similar to NADH dehydrogenase I chain A from Escherichia coli O157:H7 (13362642,). Residues 6-117 are 34% similar o NADH dehydrogenase I chain A from Pseudomonas aeruginosa strain PAO1 (gb,AAG06025.1 ...
This HMM represents a subfamily of small, transmembrane proteins believed to be components of Na+/H+ and K+/H+ antiporters. Members, including proteins designated MnhG from Staphylococcus aureus and PhaG from Rhizobium meliloti, show some similarity to chain L of the NADH dehydrogenase I, which also translocates protons ...
H+/e- stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells.: Anaerobically grown Escherichia co
Numerous significant hits using gapped BLAST to aspartokinase III from E. coli (416597), Arabidopsis thaliana (6091740, putative), Methanococcus jannaschii (2492982), among others. HD1375 is 57% similar to residues 1-449 from AK3_ECOLI ...
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In molecular biology, the amino acid kinase domain is a protein domain. It is found in protein kinases with various specificities, including the aspartate, glutamate and uridylate kinase families. In prokaryotes and plants the synthesis of the essential amino acids lysine and threonine is predominantly regulated by feed-back inhibition of aspartate kinase (AK) and dihydrodipicolinate synthase (DHPS). In Escherichia coli, thrA, metLM, and lysC encode aspartokinase isozymes that show feedback inhibition by threonine, methionine, and lysine, respectively. The lysine-sensitive isoenzyme of aspartate kinase from spinach leaves has a subunit composition of 4 large and 4 small subunits. In plants although the control of carbon fixation and nitrogen assimilation has been studied in detail, relatively little is known about the regulation of carbon and nitrogen flow into amino acids. The metabolic regulation of expression of an Arabidopsis thaliana aspartate kinase/homoserine dehydrogenase (AK/HSD) gene, ...
• The permeability of the blood-retina barrier was tested in rats with early streptozocin-induced diabetes. Two different tracer substances were used: fluoresce
Ogilvie, JW; Vickers, LP; Clark, RB; Jones, MM (1975). "Aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12 ( ... Snook, Christopher F.; Tipton, Peter A.; Beamer, Lesa J. (2003). "Crystal Structure of GDP-Mannose Dehydrogenase: A Key Enzyme ... Huang, CY; Frieden, C (1972). "The mechanism of ligand-induced structural changes in glutamate dehydrogenase. Studies of the ... Babady, N. E.; Pang, Y.-P.; Elpeleg, O.; Isaya, G. (2007). "Cryptic proteolytic activity of dihydrolipoamide dehydrogenase". ...
... aspartokinase β-aspartate semialdehyde dehydrogenase homoserine dehydrogenase homoserine kinase threonine synthase. Threonine ... Homoserine undergoes O-phosphorylation; this phosphate ester undergoes hydrolysis concomitant with relocation of the OH group. ... In humans the gene for threonine dehydrogenase is an inactive pseudogene, so threonine is converted to α-ketobutyrate. The ... In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. ...
Relevant enzymes include aspartokinase, aspartate-semialdehyde dehydrogenase, homoserine dehydrogenase, homoserine O- ... β-aspartate semialdehyde dehydrogenase, homoserine dehydrogenase, homoserine kinase, threonine synthase. The biosynthesis of ... There are two bifunctional aspartokinase/homoserine dehydrogenases, ThrA and MetL, in addition to a monofunctional ... The initial two stages of the DAP pathway are catalyzed by aspartokinase and aspartate semialdehyde dehydrogenase. These ...
... homoserine dehydrogenase MeSH D08.811.682.047.370.060 - aspartokinase homoserine dehydrogenase MeSH D08.811.682.047.385 - 3- ... aspartokinase homoserine dehydrogenase MeSH D08.811.600.200 - cholesterol side-chain cleavage enzyme MeSH D08.811.600.250 - ... aspartokinase homoserine dehydrogenase MeSH D08.811.913.696.630.700 - phosphoglycerate kinase MeSH D08.811.913.696.640 - ... malate dehydrogenase MeSH D08.811.682.047.748 - malate dehydrogenase (nadp+) MeSH D08.811.682.047.892 - xanthine dehydrogenase ...
Aspartokinase Aspartate-semialdehyde dehydrogenase Homoserine dehydrogenase Homoserine O-transsuccinylase Cystathionine-γ- ... Homoserine is the branching point with the threonine pathway, where instead it is isomerised after activating the terminal ... In most organisms, an acetyl group is used to activate the homoserine. This can be catalysed in bacteria by an enzyme encoded ... 7) The enzyme α-ketoacid dehydrogenase converts α-ketobutyrate to propionyl-CoA, which is metabolized to succinyl-CoA in a ...
The bifunctional aspartokinase-homoserine dehydrogenase (AK-HSD) enzyme has a regulatory domain that consists of two subdomains ... the precise mechanism of complete homoserine dehydrogenase catalysis remains unknown. The homoserine dehydrogenase-catalyzed ... Starnes WL, Munk P, Maul SB, Cunningham GN, Cox DJ, Shive W (1972). "Threonine-sensitive aspartokinase-homoserine dehydrogenase ... Veron M, Falcoz-Kelly F, Cohen GN (1972). "The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of ...
Zhu-Shimoni JX, Galili G (March 1998). "Expression of an arabidopsis aspartate Kinase/Homoserine dehydrogenase gene is ... Kikuchi Y, Kojima H, Tanaka T (April 1999). "Mutational analysis of the feedback sites of lysine-sensitive aspartokinase of ... The metabolic regulation of expression of an Arabidopsis thaliana aspartate kinase/homoserine dehydrogenase (AK/HSD) gene, ... and lysC encode aspartokinase isozymes that show feedback inhibition by threonine, methionine, and lysine, respectively. The ...
... homoserine biosynthetic process, lysine biosynthetic process via diaminopimelate ... Bifunctional aspartokinase/homoserine dehydrogenase 1. Alternative name(s):. Aspartokinase I/homoserine dehydrogenase I. Short ... Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL) ... Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL) ...
Recombinant Protein and Bifunctional aspartokinase/homoserine dehydrogenase Antibody at MyBioSource. Custom ELISA Kit, ... Bifunctional aspartokinase/homoserine dehydrogenase 1. Bifunctional aspartokinase/homoserine dehydrogenase 1 ELISA Kit. ... Bifunctional aspartokinase/homoserine dehydrogenase 2. Bifunctional aspartokinase/homoserine dehydrogenase 2 ELISA Kit. ... Bifunctional aspartokinase/homoserine dehydrogenase. Bifunctional aspartokinase/homoserine dehydrogenase ELISA Kit. ...
Ogilvie, JW; Vickers, LP; Clark, RB; Jones, MM (1975). "Aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12 ( ... Snook, Christopher F.; Tipton, Peter A.; Beamer, Lesa J. (2003). "Crystal Structure of GDP-Mannose Dehydrogenase: A Key Enzyme ... Huang, CY; Frieden, C (1972). "The mechanism of ligand-induced structural changes in glutamate dehydrogenase. Studies of the ... Babady, N. E.; Pang, Y.-P.; Elpeleg, O.; Isaya, G. (2007). "Cryptic proteolytic activity of dihydrolipoamide dehydrogenase". ...
Expression of Aspartokinase, Dihydrodipicolinic Acid Synthase and Homoserine Dehydrogenase During Growth of Carrot Cell ...
The bifunctional aspartokinase-homoserine dehydrogenase (AK-HSD) enzyme has a regulatory domain that consists of two subdomains ... the precise mechanism of complete homoserine dehydrogenase catalysis remains unknown. The homoserine dehydrogenase-catalyzed ... Starnes WL, Munk P, Maul SB, Cunningham GN, Cox DJ, Shive W (1972). "Threonine-sensitive aspartokinase-homoserine dehydrogenase ... Veron M, Falcoz-Kelly F, Cohen GN (1972). "The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of ...
Relevant enzymes include aspartokinase, aspartate-semialdehyde dehydrogenase, homoserine dehydrogenase, homoserine O- ... β-aspartate semialdehyde dehydrogenase, homoserine dehydrogenase, homoserine kinase, threonine synthase. ... There are two bifunctional aspartokinase/homoserine dehydrogenases, ThrA and MetL, in addition to a monofunctional ... The initial two stages of the DAP pathway are catalyzed by aspartokinase and aspartate semialdehyde dehydrogenase. These ...
"Transcriptional and biochemical regulation of a novel Arabidopsis thaliana bifunctional aspartate kinase-homoserine ... dehydrogenase gene isolated by functional complementation of a yeast hom6 mutant, Plant Molecular Biology" on DeepDyve, the ... Bifunctional protein in carrot contains both aspartokinase and homoserine dehydrogenase activities. Wilson, B.J.; Gray, A.C.; ... Identification and ex-pression of a cDNA from Daucus carota encoding a bifunctional aspartokinase-homoserine dehydrogenase ...
... homoserine dehydrogenase 1 [EC:2.7.2.4 1.1.1.3] K12525 metL; bifunctional aspartokinase / homoserine dehydrogenase 2 [EC:2.7. ... BSQ33_06795 lysine-sensitive aspartokinase 3 BSQ33_05150 bifunctional aspartate kinase/homoserine dehydrogenase I BSQ33_10105 ... bifunctional aspartate kinase/homoserine dehydrogenase II K00928 lysC; aspartate kinase [EC:2.7.2.4] K00928 lysC; aspartate ... kinase [EC:2.7.2.4] K00928 lysC; aspartate kinase [EC:2.7.2.4] K12524 thrA; bifunctional aspartokinase / ...
Role of serine 352 in the allosteric response of Serratia marcescens aspartokinase I-homoserine dehydrogenase I analyzed by ...
L-homoserine:NADP+ oxidoreductase, EC 1.1.1.3) has been cloned and its nucleotide sequence ... subtilis homoserine dehydrogenase shows extensive similarity with the C-terminal part of E. coli aspartokinases-homoserine ... subtilis aspartokinases and E. coli aspartokinases-homoserine dehydrogenases stops. These data suggest that the E. coli ... Structural and evolutionary relationships with Escherichia coli aspartokinases-homoserine dehydrogenases I and II. ...
... aspartate semialdehyde dehydrogenase gene (asd), aspartokinase I-homoserine dehydrogenase gene (thrA), homoserine kinase gene ( ... feedback inhibition of aspartokinase 1-homoserine dehydrogenase I encoded by thrA in the threonine operon by L-threonine is ... The kat-13 strain is resistant to borrelidin, has homoserine dehydrogenase which is not subject to feedback inhibition by L- ... The 427T23 strain has homoserine dehydrogenase which is not subject to feedback inhibition by L-threonine. Also, this strain ...
Bifunctional aspartokinase/homoserine dehydrogenase II 11173. EC. - - 70.8. 24034 Glyceraldehyde-3-phosphate dehydrogenase, ...
... aspartokinase I and homoserine dehydrogenase I) and MetL (aspartokinase II and homoserine dehydrogenase II) where only the ... Truffa-Bachi P, Van Rapenbusch R, Gros C, Cohen GN, Janin J: The threonine-sensitive homoserine dehydrogenase and aspartokinase ... Vickers LP, Ackers GK, Ogilvie JW: Aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12. Concentration-dependent ... Both the amino-terminal aspartokinase and the carboxy-terminal homoserine dehydrogenase activities of ThrA and MetL have been ...
... aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to ... Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within ... Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely ... such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate ...
... encoding aspartokinase/homoserine dehydrogenase) were kindly provided by A. Allen (University of Cambridge, Cambridge, United ...
1.1.1.3 homoserine dehydrogenase. K12525 metL; bifunctional aspartokinase / homoserine dehydrogenase 2. 2. Transferases. 2.7 ... homoserine dehydrogenase 2. 00300 Lysine biosynthesis. K12525 metL; bifunctional aspartokinase / homoserine dehydrogenase 2. ... the bifunctional aspartokinase ii-homoserine dehydrogenase II, and the bifunctional product of the thrA gene, aspartokinase I- ... K12525 metL; bifunctional aspartokinase / homoserine dehydrogenase 2. Enzymes [BR:ko01000]. 1. Oxidoreductases. 1.1 Acting on ...
... an aspartokinase/homoserine dehydrogenase, a glucose kinase, and a DNA mismatch repair enzyme, respectively (8). PCR products ... Bacterial cytotoxicity was evaluated by lactate dehydrogenase measurement with Cyto-Tox 96 Cytoxicity Kit (Promega, Madison, WI ...
... locus near a gene encoding aspartokinase homoserine dehydrogenase (AK-HSDH) and also near the I locus affecting seed coat color ...
... "aspartokinase/homoserine dehydrogenase" FT /gene_family="HOG000271594" [ FAMILY / ALN / TREE ] FT /codon_start="1" FT /locus_ ... "homoserine/homoserine lactone efflux protein" FT /transl_table="11" FT /db_xref="GI:320154959" FT /db_xref="GeneID:10164819" FT ... "dihydrolipoamide dehydrogenase of pyruvate FT /gene_family="HOG000276708" [ FAMILY / ALN / TREE ] FT dehydrogenase complex" FT ... dehydrogenase" FT /codon_start="1" FT /locus_tag="VVM_00226" FT /EC_number="1.2.1.12" FT /db_xref="GI:320154962" FT /db_xref=" ...
gi,16763392,ref,NP_459007.1, bifunctional aspartokinase I/homoserine dehydrogenase I (STM0002) [Salmonella enterica subsp. ... gi,16763393,ref,NP_459008.1, homoserine kinase (STM0003) [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2] ( ...
J.K. Bryan, Studies on the catalytic and regulatory properties of homoserine dehydrogenase of Zea mays roots, Biochim. Biophys ... K.F. Wong and D.T. Dennis, Aspartokinase from wheat germ. Isolation, characterization and regulation, Plant Physiol. 51:322-326 ...
gi,16127996,ref,NP_414543.1, fused aspartokinase I and homoserine dehydrogenase I (thrA b0002 exp) [Escherichia coli str. K-12 ... gi,16127997,ref,NP_414544.1, homoserine kinase (thrB b0003 exp) [Escherichia coli str. K-12 substr. MG1655] 310. H.sapiens. 1- ...
aspartokinase. *β-aspartate semialdehyde dehydrogenase. *homoserine dehydrogenase. *homoserine acyltransferase. *cystathionine- ... Homoserine converts to O-succinyl homoserine, which then reacts with cysteine to produce cystathionine, which is cleaved to ... 7) α-ketoacid dehydrogenase converts α-ketobutyrate to propionyl-CoA, which is metabolized to succinyl-CoA in a three-step ... First, aspartic acid is converted via β-aspartyl-semialdehyde into homoserine, introducing the pair of contiguous methylene ...
aspartokinase. *α-aspartate semialdehyde dehydrogenase. *homoserine dehydrogenase. *homoserine kinase. *threonine synthase. ... Homoserine undergoes O-phosphorylation; this phosphate ester undergoes hydrolysis concomitant with relocation of the OH group ( ... In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. ...
Acetobacter aceti possesses one aspartokinase and a separate homoserine dehydrogenase. Neither enzyme is subject to repression ... Aspartokinase was inhibited by l-threonine or l-lysine and concertedly inhibited by the two together. l-Methionine or l- ... SUMMARY: Growth of Acetobacter aceti NCIB8554 was inhibited by l-threonine and l-homoserine. Inhibition was relieved by l- ... Growth Inhibition of Acetobacter aceti by L-Threonine and L-Homoserine: the Primary Regulation of the Biosynthesis of Amino ...
Interestingly, despite the presence of a CBS, we could not find a gene(s) encoding aspartokinase or homoserine dehydrogenase in ... NADH dehydrogenase subunit 5, and glyceraldehyde-3-phosphate dehydrogenase were selected as standards. The stabilities of these ... 1987 Localization of two L-glutamate dehydrogenases in the coral Acropora latistella. Arch. Biochem. Biophys. 254: 368-371. ... For UniProt and transcript numbers, see Table S5, lines 1-4. The possible localizations of the glutamate dehydrogenases are ...
aspartokinase * α-aspartate semialdehyde dehydrogenase * homoserine dehydrogenase * homoserine kinase * threonine synthase. ... Homoserine undergoes O-phosphorylation; this phosphate ester undergoes hydrolysis concomitant with relocation of the OH group.[ ... It is converted to pyruvate via Threonine Dehydrogenase. An intermediate in this pathway can undergo thiolysis with CoA to ... In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. ...
Homoserine dehydrogenase 0.999. RB2654_20473. RB2654_22308. RB2654_20473. RB2654_22308. Aspartokinase ... Aspartokinase Ornithine carbamoyltransferase ; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl ...
Aspartokinase homoserine dehydrogenase Entry term(s):. Aspartokinase I Homoserine Dehydrogenase I. Aspartokinase II Homoserine ... Dehydrogenase, Bifunctional Aspartokinase-Homoserine Homoserine Dehydrogenase, Aspartokinase Aspartokinase II Homoserine ... Dehydrogenase, Aspartokinase Homoserine. Dehydrogenase, Bifunctional Aspartokinase-Homoserine. Homoserine Dehydrogenase, ... Bifunctional Aspartokinase Homoserine Dehydrogenase 2 Bifunctional Aspartokinase-Homoserine Dehydrogenase 2 Aspartokinase I ...
Enzyme A is aspartokinase; B, homoserine dehydrogenase; C, threonine dehydratase. Dr. Nikhat Siddiqi ... from homoserine, from aspartate -semialdehyde, and from aspartate (steps 4 , 3 , and 1 in Fig.). This overall regulatory ... semialdehyde to homoserine and from threonine to -ketobutyrate are also catalyzed by dual, independently controlled isozymes. ...
  • Aspartate kinase II / homoserine dehydrogenase II (MetL) is a bifunctional enzyme that catalyzes the first step in the biosynthesis of lysine and homoserine, and indirectly methionine and threonine, as well as catalyzing the final step in homoserine biosynthesis. (mybiosource.com)
  • The AK-HSD gene codes for aspartate kinase, an intermediate domain (coding for the linker region between the two enzymes in the bifunctional form), and finally the coding sequence for homoserine dehydrogenase. (wikipedia.org)
  • Additionally, the aspartate kinase-homoserine dehydrogenase gene is primarily expressed in actively growing, young plant tissues, particularly in the apical and lateral meristems. (wikipedia.org)
  • Homoserine dehydrogenase and aspartate kinase are both subject to significant regulation (refer to figure 3). (wikipedia.org)
  • Frankard, Valérie 2004-10-17 00:00:00 An aspartate kinase-homoserine dehydrogenase (AK-HSDH) cDNA of Arabidopsis thaliana has been cloned by functional complementation of a Saccharomyces cerevisiae strain mutated in its homoserine dehydrogenase (HSDH) gene (hom6). (deepdyve.com)
  • 5. The method according to claim 4, wherein the L-threonine biosynthesis enzyme is selected from the group consisting of aspartokinase, homoserine kinase, threonine synthase, and combinations thereof. (freepatentsonline.com)
  • Nucleotide sequence analysis indicates that the hom stop codon overlaps the start codon of thrC (threonine synthase) suggesting that these genes, as well as thrB (homoserine kinase) located downstream from thrC, belong to the same transcription unit. (pasteur.fr)
  • homoserine kinase (STM0003) [Salmonella enterica subsp. (burnham.org)
  • homoserine kinase (thrB b0003 exp ) [Escherichia coli str. (burnham.org)
  • The metabolic regulation of expression of an Arabidopsis thaliana aspartate kinase/homoserine dehydrogenase (AK/HSD) gene, which encodes two linked key enzymes in the biosynthetic pathway of aspartate family amino acids has been studied [ PMID: 9501134 ]. (ebi.ac.uk)
  • homoserine kinase [Campylobacter jejuni subsp. (godziklab.org)
  • Complementation studies showed that thethrB gene (encoding homoserine kinase) is found downstream from thethrC gene, and analysis of nucleotide sequences indicated that thehom gene (encoding homoserine dehydrogenase) is located upstream of thethrC gene. (naver.com)
  • Residues 119-293 are 75% similar to a (KINASE ASPARTOKINASE BIOSYNTHESIS) protein domain (PD000447) which is seen in Q9CM97_PASMU. (northwestern.edu)
  • homoserine kinase (STY0003) [Salmonella enterica subsp. (godziklab.org)
  • ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). (nih.gov)
  • fused aspartokinase I and homoserine dehydrogenase I (thrA b0002 exp ) [Escherichia coli str. (burnham.org)
  • In Escherichia coli three different aspartokinases (AKI, AKII, AKIII, the products of thrA , metL and lysC , respectively) can perform the first step of the CP. (biomedcentral.com)
  • The enzyme can also be found in a bifunctional form consisting of an N-terminal aspartokinase domain and a C-terminal homoserine dehydrogenase domain, as found in bacteria such as Escherichia coli and in plants. (wikipedia.org)
  • The B. subtilis enzyme expressed in Escherichia coli is sensitive by inhibition by threonine and allows complementation of a strain lacking homoserine dehydrogenases I and II. (pasteur.fr)
  • Mutational analysis of the feedback sites of lysine-sensitive aspartokinase of Escherichia coli. (ebi.ac.uk)
  • The asd gene, encoding the enzyme aspartic semialdehyde dehydrogenase, has been cloned by complementation of Escherichia coli asd mutants. (microbiologyresearch.org)
  • The combination of Bacillus subtilis threonine deaminase and a mutated Escherichia coli glutamate dehydrogenase resulted in the intracellular accumulation of 0.40 mg/L of ( S )-2-aminobutyric acid. (biomedcentral.com)
  • Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. (pasteur.fr)
  • The Bacillus subtilis hom gene, encoding homoserine dehydrogenase (L-homoserine:NADP+ oxidoreductase, EC 1.1.1.3) has been cloned and its nucleotide sequence determined. (pasteur.fr)
  • Soybean ( Glycine max L. Merrill) linkage group A2 contains a major resistance gene to the soybean cyst nematode ( Heterodera glycines Ichinohe) at the Rhg 4 locus near a gene encoding aspartokinase homoserine dehydrogenase (AK-HSDH) and also near the I locus affecting seed coat color. (springer.com)
  • The ask gene encoding the aspartokinase (Ask) is located upstream of the asd gene as shown by determination of Ask activity conferred to E. coli transformants. (microbiologyresearch.org)
  • synthase and/or O-acetyl homoserine sulfhydrylase encoded by the METB gene of Saccharomyces cerevisiae. (patentsencyclopedia.com)
  • Lactic acid (2-hydroxypropanoic acid) is synthesized in one step from pyruvate, the end product of the glycolytic pathway, by lactate dehydrogenase (LDH), which is encoded by the ldhA gene (Fig. 1 ). (biomedcentral.com)
  • Cloning and nucleotide sequences of the homoserine dehydrogenase genes (hom) and the threonine synthase genes (thrC) of the gram-negative obligate methylotroph Methylobacillus glycogenes. (naver.com)
  • Homoserine is an intermediate in the biosynthesis of threonine, isoleucine, and methionine. (wikipedia.org)
  • View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homoserine from L-aspartate , the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis . (uniprot.org)
  • Homoserine can be then channeled towards threonine and/or methionine biosyntheses. (biomedcentral.com)
  • The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. (nih.gov)
  • A bifunctional protein consisting of aspartokinase, and homoserine dehydrogenase activities. (bvsalud.org)
  • This protein is involved in step 3 of the subpathway that synthesizes L-homoserine from L-aspartate. (uniprot.org)
  • The systematic name of this enzyme class is L-homoserine:NAD(P)+ oxidoreductase. (wikipedia.org)
  • 1. A coryneform bacterium which has a DNA sequence coding for an aspartokinase which is desensitized in feedback inhibition by L-Lysine and L-Threonine and in which the intracellular enzymatic activities of dihydrodipicolinate reductase, dihydrodipicolinate synthase, diaminopimelate decarboxylase and diaminopimelate dehydrogenase are raised by increasing a copy number of the DNA sequences coding for said enzymes. (epo.org)
  • Homoserine dehydrogenase catalyzes an intermediate step in this nitrogen and carbon storage and utilization pathway. (wikipedia.org)
  • Mammals lack the enzymes involved in the aspartate metabolic pathway, including homoserine dehydrogenase. (wikipedia.org)
  • Glutamate dehydrogenase catalyzes the reductive amination of α-ketoglutarate to glutamate. (wikipedia.org)
  • The regulation of the synthesis of glutamate from α-ketoglutarate is subject to regulatory control of the Citric Acid Cycle as well as mass action dependent on the concentrations of reactants involved due to the reversible nature of the transamination and glutamate dehydrogenase reactions. (wikipedia.org)
  • The combination of a threonine deaminase from Solanum lycopersicum (tomato) with two copies of mutated glutamate dehydrogenase from E. coli resulted in the accumulation of comparable amounts of ( S )-2-aminobutyric acid. (biomedcentral.com)
  • You have previously studied the oxidative deamination of glutamate by glutamate dehydrogenase, in which NH 3 and a- ketoglutarate are produced. (rpi.edu)
  • The B. subtilis homoserine dehydrogenase has a C-terminal extension of about 100 residues (relative to the E. coli enzymes) that could be involved in the regulation of the enzyme activity. (pasteur.fr)
  • First, aspartic acid is converted via β-aspartyl-semialdehyde into homoserine, introducing the pair of contiguous methylene groups. (newworldencyclopedia.org)
  • In plants and microorganisms , threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. (newworldencyclopedia.org)
  • CATALYTIC ACTIVITY: L-homoserine + NAD(P)(+) = L-aspartate 4-semialdehyde + NAD(P)H. (mybiosource.com)
  • J.K. Bryan, Studies on the catalytic and regulatory properties of homoserine dehydrogenase of Zea mays roots , Biochim. (springer.com)
  • Isolation and characterization of the aspartokinase and aspartate semialdehyde dehydrogenase operon from mycobacteria. (microbiologyresearch.org)
  • Structure of the ask-asd operon and formation of aspartokinase subunits in the cephamycin producer 'Amycolatopsis lactamdurans'The GenBank accession number for the sequence reported in this paper is AJ298904. (microbiologyresearch.org)
  • In enzymology, a homoserine dehydrogenase (EC 1.1.1.3) is an enzyme that catalyzes the chemical reaction L-homoserine + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } L-aspartate 4-semialdehyde + NAD(P)H + H+ The 2 substrates of this enzyme are L-homoserine and NAD+ (or NADP+), whereas its 3 products are L-aspartate 4-semialdehyde, NADH (or NADPH), and H+. (wikipedia.org)
  • this similarity starts at the exact point where the similarity between E. coli or B. subtilis aspartokinases and E. coli aspartokinases-homoserine dehydrogenases stops. (pasteur.fr)
  • It contains enoyl-CoA hydratase, long-chain-3-hydroxyacyl-CoA dehydrogenase, and acetyl-CoA C-acyltransferase activities and plays an important role in the metabolism of long chain FATTY ACIDS. (childrensmercy.org)
  • for example, isoleucine inhibits the conversion of threonine to -ketobutyrate and threonine inhibits its own formation at three points: from homoserine, from aspartate -semialdehyde, and from aspartate (steps 4 , 3 , and 1 in Fig.). This overall regulatory mechanism is called sequential feedback inhibition. (slideplayer.com)
  • Homoserine dehydrogenase also exhibits multi-order kinetics at subsaturating levels of substrate. (wikipedia.org)
  • Additionally, the variable kinetics for homoserine dehydrogenase is an artifact of the faster dissociation of the amino acid substrate from the enzyme complex as compared to cofactor dissociation. (wikipedia.org)
  • 5. Theorell, H. Kinetics and equilibria in the liver alcohol dehydrogenase system. (qmul.ac.uk)
  • These data suggest that the E. coli bifunctional polypeptide could have resulted from the direct fusion of ancestral aspartokinase and homoserine dehydrogenase. (pasteur.fr)
  • Homoserine dehydrogenase catalyzes the reaction of aspartate-semialdehyde (ASA) to homoserine. (wikipedia.org)
  • Aspartokinase II-homoserine dehydrogenase II and aspartokinase III also catalyze the same reaction(s). (uniprot.org)
  • The homoserine dehydrogenase-catalyzed reaction has been postulated to proceed through a bi-bi kinetic mechanism, where the NAD(P)H cofactor binds the enzyme first and is the last to dissociate from the enzyme once the reaction is complete. (wikipedia.org)
  • It is converted to pyruvate via Threonine Dehydrogenase. (bionity.com)
  • Homoserine converts to O -succinyl homoserine, which then reacts with cysteine to produce cystathionine, which is cleaved to yield homocysteine. (newworldencyclopedia.org)
  • Homoserine dehydrogenase has an NAD(P)H cofactor, which then donates a hydrogen to the same carbon, effectively reducing the aldehyde to an alcohol. (wikipedia.org)
  • The bifunctional aspartokinase-homoserine dehydrogenase (AK-HSD) enzyme has a regulatory domain that consists of two subdomains with a common loop-alpha helix-loop-beta strand loop-beta strand motif. (wikipedia.org)
  • The archetypical ACT domain is the C-terminal regulatory domain of 3-phosphoglycerate dehydrogenase (3PGDH), which folds with a ferredoxin-like topology. (ebi.ac.uk)